We continued solution scattering measurements of the wild-type and mutant P22 capsid. Instrument calibration was done more carefully this time than last year, and we observed scattering peaks whose Bragg spacing match very well with those calculated from the EM structures that the Baylor group had obtained. In the higher angle region, we have a few characteristic peaks that may arise from b-sheet structure of the capsid protein and/or from RNA packing inside. We measured solution x-ray scattering from the scaffolding protein in the temperature range 15 - 60 0C. Clear changes in the assembly state of the scaffolding protein were seen in subsidiary scattering peaks. The studies were continued on a separate experimental proposal by W. Chiu et al.